ID TRPC_CORGL Reviewed; 474 AA. AC P06560; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 26-JUL-2002, sequence version 2. DT 27-MAR-2024, entry version 149. DE RecName: Full=Tryptophan biosynthesis protein TrpCF; DE Includes: DE RecName: Full=Indole-3-glycerol phosphate synthase; DE Short=IGPS; DE EC=4.1.1.48; DE Includes: DE RecName: Full=N-(5'-phospho-ribosyl)anthranilate isomerase; DE Short=PRAI; DE EC=5.3.1.24; GN Name=trpC; Synonyms=trpCF; OrderedLocusNames=Cgl3033, cg3362; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / OS JCM 1318 / LMG 3730 / NCIMB 10025). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196627; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3808947; DOI=10.1093/nar/14.24.10113; RA Matsui K., Sano K., Ohtsubo E.; RT "Complete nucleotide and deduced amino acid sequences of the Brevibacterium RT lactofermentum tryptophan operon."; RL Nucleic Acids Res. 14:10113-10114(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its RT impact on the production of L-aspartate-derived amino acids and vitamins."; RL J. Biotechnol. 104:5-25(2003). CC -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of CC tryptophan biosynthetic pathway. The first reaction is catalyzed by the CC isomerase, coded by the TrpF domain; the second reaction is catalyzed CC by the synthase, coded by the TrpC domain (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2- CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; CC EC=5.3.1.24; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) CC = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O; CC Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 4/5. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: In the N-terminal section; belongs to the TrpC family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the TrpF family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04960; CAA28626.1; -; Genomic_DNA. DR EMBL; BA000036; BAC00427.1; -; Genomic_DNA. DR EMBL; BX927157; CAF18973.1; -; Genomic_DNA. DR PIR; E24723; E24723. DR RefSeq; NP_602226.2; NC_003450.3. DR RefSeq; WP_011015582.1; NC_006958.1. DR PDB; 7ETX; X-ray; 2.10 A; A=1-474. DR PDB; 7ETY; X-ray; 2.21 A; A/B=1-474. DR PDBsum; 7ETX; -. DR PDBsum; 7ETY; -. DR AlphaFoldDB; P06560; -. DR SMR; P06560; -. DR STRING; 196627.cg3362; -. DR KEGG; cgb:cg3362; -. DR KEGG; cgl:Cgl3033; -. DR PATRIC; fig|196627.13.peg.2967; -. DR eggNOG; COG0134; Bacteria. DR eggNOG; COG0135; Bacteria. DR HOGENOM; CLU_007713_1_1_11; -. DR OrthoDB; 9766131at2; -. DR BioCyc; CORYNE:G18NG-12654-MONOMER; -. DR UniPathway; UPA00035; UER00042. DR UniPathway; UPA00035; UER00043. DR Proteomes; UP000000582; Chromosome. DR Proteomes; UP000001009; Chromosome. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00331; IGPS; 1. DR CDD; cd00405; PRAI; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 2. DR HAMAP; MF_00135; PRAI; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR045186; Indole-3-glycerol_P_synth. DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom. DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS. DR InterPro; IPR001240; PRAI_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR PANTHER; PTHR22854:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1. DR Pfam; PF00218; IGPS; 1. DR Pfam; PF00697; PRAI; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2. DR PROSITE; PS00614; IGPS; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Decarboxylase; Isomerase; Lyase; Multifunctional enzyme; KW Reference proteome; Tryptophan biosynthesis. FT CHAIN 1..474 FT /note="Tryptophan biosynthesis protein TrpCF" FT /id="PRO_0000154276" FT REGION 1..262 FT /note="Indole-3-glycerol phosphate synthase" FT REGION 263..474 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT CONFLICT 88..89 FT /note="SG -> AA (in Ref. 1; CAA28626)" FT /evidence="ECO:0000305" FT CONFLICT 110 FT /note="A -> G (in Ref. 1; CAA28626)" FT /evidence="ECO:0000305" FT CONFLICT 130..131 FT /note="HA -> RP (in Ref. 1; CAA28626)" FT /evidence="ECO:0000305" FT CONFLICT 153 FT /note="A -> D (in Ref. 1; CAA28626)" FT /evidence="ECO:0000305" FT CONFLICT 302 FT /note="L -> S (in Ref. 1; CAA28626)" FT /evidence="ECO:0000305" FT CONFLICT 343 FT /note="D -> G (in Ref. 1; CAA28626)" FT /evidence="ECO:0000305" FT CONFLICT 381..383 FT /note="Missing (in Ref. 1; CAA28626)" FT /evidence="ECO:0000305" FT CONFLICT 454..474 FT /note="AGAKDAGALLKIFATISTFHY -> GWGERCRRAAENFRDHLHIPLLKV FT (in Ref. 1; CAA28626)" FT /evidence="ECO:0000305" FT HELIX 8..18 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 21..27 FT /evidence="ECO:0007829|PDB:7ETX" FT TURN 28..30 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 33..35 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 43..48 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 55..60 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:7ETY" FT TURN 65..67 FT /evidence="ECO:0007829|PDB:7ETY" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:7ETY" FT HELIX 76..83 FT /evidence="ECO:0007829|PDB:7ETX" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 88..93 FT /evidence="ECO:0007829|PDB:7ETX" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 103..112 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 126..134 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 138..143 FT /evidence="ECO:0007829|PDB:7ETX" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 149..161 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 165..169 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 173..181 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 185..192 FT /evidence="ECO:0007829|PDB:7ETX" FT TURN 194..196 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 202..208 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 215..221 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 226..232 FT /evidence="ECO:0007829|PDB:7ETX" FT TURN 233..235 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 243..246 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 251..259 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 271..280 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 283..288 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 299..308 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 312..318 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 324..327 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 332..337 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 345..359 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 363..370 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 376..383 FT /evidence="ECO:0007829|PDB:7ETX" FT TURN 384..386 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 388..393 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 397..399 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 405..407 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 410..414 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 416..421 FT /evidence="ECO:0007829|PDB:7ETX" FT TURN 424..426 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 427..432 FT /evidence="ECO:0007829|PDB:7ETX" FT STRAND 436..441 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 442..444 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 448..453 FT /evidence="ECO:0007829|PDB:7ETX" FT HELIX 459..471 FT /evidence="ECO:0007829|PDB:7ETX" SQ SEQUENCE 474 AA; 50477 MW; C347C7016BB97F9A CRC64; MTSNNLPTVL ESIVEGRRGH LEEIRARIAH VDVDALPKST RSLFDSLNQG RGGARFIMEC KSASPSLGMI REHYQPGEIA RVYSRYASGI SVLCEPDRFG GDYDHLATVA ATSHLPVLCK DFIIDPVQVH AARYFGADAI LLMLSVLDDE EYAALAAEAA RFDLDILTEV IDEEEVARAI KLGAKIFGVN HRNLHDLSID LDRSRRLSKL IPADAVLVSE SGVRDTETVR QLGGHSNAFL VGSQLTSQEN VDLAARELVY GPNKVCGLTS PSAAQTARAA GAVYGGLIFE EASPRNVSRE TLQKIIAAEP NLRYVAVSRR TSGYKDLLVD GIFAVQIHAP LQDSVEAEKA LIAAVREEVG PQVQVWRAIS MSSPLGAEVA AAVEGDVDKL ILDAHEGGSG EVFDWATVPA AVKAKSLLAG GISPDNAAQA LAVGCAGLDI NSGVEYPAGA GTWAGAKDAG ALLKIFATIS TFHY //